1ioj

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[[Image:1ioj.gif|left|200px]]
 
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{{Structure
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==HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES==
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|PDB= 1ioj |SIZE=350|CAPTION= <scene name='initialview01'>1ioj</scene>
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<StructureSection load='1ioj' size='340' side='right'caption='[[1ioj]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1ioj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IOJ FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ioj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ioj OCA], [https://pdbe.org/1ioj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ioj RCSB], [https://www.ebi.ac.uk/pdbsum/1ioj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ioj ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES'''
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[https://www.uniprot.org/uniprot/APOC1_HUMAN APOC1_HUMAN] Appears to modulate the interaction of APOE with beta-migrating VLDL and inhibit binding of beta-VLDL to the LDL receptor-related protein. Binds free fatty acids and reduces their intracellular esterification.<ref>PMID:17339654</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we present the nuclear magnetic resonance spectra of native apoC-I and synthetic apoC-I, containing selected 15N-labelled amino acids, in the presence of sodium dodecyl sulfate. The proton resonances of apoC-I are assigned and the secondary structure is estimated from the difference of measured alpha-proton chemical shifts to random coil values and the observed NOE interactions. According to these data apoC-I forms two helices, Val-4-Lys-30 and Leu-34-Lys-52, linked by an unstructured region Gln-31-Glu-33. The N-terminal segments of each helix, Val-4-Gly-15 and Leu-34-Met-38, appear to be more flexible than the helical core regions Asn-16-Lys-30 and Arg-39-Lys-52.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/io/1ioj_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1IOJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOJ OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ioj ConSurf].
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Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate., Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ, Biochem Cell Biol. 1998;76(2-3):267-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9923695 9923695]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cushley, R J.]]
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[[Category: Cushley RJ]]
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[[Category: Rozek, A.]]
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[[Category: Rozek A]]
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[[Category: Sparrow, J T.]]
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[[Category: Sparrow JT]]
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[[Category: Weisgraber, K H.]]
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[[Category: Weisgraber KH]]
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[[Category: amphipathic helix]]
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[[Category: apolipoprotein]]
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[[Category: lcat activation]]
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[[Category: lipid association]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:56 2008''
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Current revision

HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES

PDB ID 1ioj

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